INT12_MOUSE
ID INT12_MOUSE Reviewed; 461 AA.
AC Q9D168; Q3U2Q5; Q921U2;
DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Integrator complex subunit 12;
DE Short=Int12;
DE AltName: Full=PHD finger protein 22;
GN Name=Ints12; Synonyms=Phf22;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD; TISSUE=Embryo;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Eye, Mammary gland, and Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP STRUCTURE BY NMR OF 150-224.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of PHD domain in protein NP_082203.";
RL Submitted (NOV-2004) to the PDB data bank.
CC -!- FUNCTION: Component of the Integrator complex, a complex involved in
CC the small nuclear RNAs (snRNA) U1 and U2 transcription and in their 3'-
CC box-dependent processing. The Integrator complex is associated with the
CC C-terminal domain (CTD) of RNA polymerase II largest subunit (POLR2A)
CC and is recruited to the U1 and U2 snRNAs genes. Mediates recruitment of
CC cytoplasmic dynein to the nuclear envelope, probably as component of
CC the INT complex. {ECO:0000250|UniProtKB:Q96CB8}.
CC -!- SUBUNIT: Belongs to the multiprotein complex Integrator, at least
CC composed of INTS1, INTS2, INTS3, INTS4, INTS5, INTS6, INTS7, INTS8,
CC INTS9/RC74, INTS10, INTS11/CPSF3L and INTS12.
CC {ECO:0000250|UniProtKB:Q96CB8}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q96CB8}.
CC -!- SIMILARITY: Belongs to the Integrator subunit 12 family. {ECO:0000305}.
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DR EMBL; AK003874; BAB23052.1; -; mRNA.
DR EMBL; AK155162; BAE33085.1; -; mRNA.
DR EMBL; BC010657; AAH10657.1; -; mRNA.
DR EMBL; BC023801; AAH23801.1; -; mRNA.
DR EMBL; BC046996; AAH46996.1; -; mRNA.
DR CCDS; CCDS17848.1; -.
DR RefSeq; NP_082203.1; NM_027927.4.
DR PDB; 1WEV; NMR; -; A=150-224.
DR PDBsum; 1WEV; -.
DR AlphaFoldDB; Q9D168; -.
DR SMR; Q9D168; -.
DR STRING; 10090.ENSMUSP00000029650; -.
DR iPTMnet; Q9D168; -.
DR PhosphoSitePlus; Q9D168; -.
DR EPD; Q9D168; -.
DR jPOST; Q9D168; -.
DR MaxQB; Q9D168; -.
DR PaxDb; Q9D168; -.
DR PeptideAtlas; Q9D168; -.
DR PRIDE; Q9D168; -.
DR ProteomicsDB; 268974; -.
DR Antibodypedia; 26162; 79 antibodies from 22 providers.
DR Ensembl; ENSMUST00000029650; ENSMUSP00000029650; ENSMUSG00000028016.
DR GeneID; 71793; -.
DR KEGG; mmu:71793; -.
DR UCSC; uc008rkj.1; mouse.
DR CTD; 57117; -.
DR MGI; MGI:1919043; Ints12.
DR VEuPathDB; HostDB:ENSMUSG00000028016; -.
DR eggNOG; KOG4323; Eukaryota.
DR GeneTree; ENSGT00390000005218; -.
DR HOGENOM; CLU_033336_0_0_1; -.
DR InParanoid; Q9D168; -.
DR OMA; AKQDKRN; -.
DR OrthoDB; 1631937at2759; -.
DR PhylomeDB; Q9D168; -.
DR TreeFam; TF106418; -.
DR Reactome; R-MMU-6807505; RNA polymerase II transcribes snRNA genes.
DR BioGRID-ORCS; 71793; 8 hits in 62 CRISPR screens.
DR ChiTaRS; Ints12; mouse.
DR EvolutionaryTrace; Q9D168; -.
DR PRO; PR:Q9D168; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q9D168; protein.
DR Bgee; ENSMUSG00000028016; Expressed in secondary oocyte and 247 other tissues.
DR Genevisible; Q9D168; MM.
DR GO; GO:0032039; C:integrator complex; ISS:HGNC-UCL.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0034472; P:snRNA 3'-end processing; IBA:GO_Central.
DR GO; GO:0016180; P:snRNA processing; ISS:HGNC-UCL.
DR CDD; cd15501; PHD_Int12; 1.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR039053; Int12.
DR InterPro; IPR039054; Int12_PHD.
DR InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR019787; Znf_PHD-finger.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR13415:SF4; PTHR13415:SF4; 1.
DR Pfam; PF00628; PHD; 1.
DR SMART; SM00249; PHD; 1.
DR SUPFAM; SSF57903; SSF57903; 1.
DR PROSITE; PS01359; ZF_PHD_1; 1.
DR PROSITE; PS50016; ZF_PHD_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Isopeptide bond; Metal-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..461
FT /note="Integrator complex subunit 12"
FT /id="PRO_0000059314"
FT ZN_FING 158..214
FT /note="PHD-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT REGION 42..131
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 302..443
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 55..86
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 88..123
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 302..356
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 370..443
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 127
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96CB8"
FT CROSSLNK 68
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q96CB8"
FT CROSSLNK 253
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q96CB8"
FT HELIX 154..157
FT /evidence="ECO:0007829|PDB:1WEV"
FT STRAND 162..164
FT /evidence="ECO:0007829|PDB:1WEV"
FT STRAND 175..177
FT /evidence="ECO:0007829|PDB:1WEV"
FT STRAND 179..181
FT /evidence="ECO:0007829|PDB:1WEV"
FT STRAND 184..186
FT /evidence="ECO:0007829|PDB:1WEV"
FT TURN 187..189
FT /evidence="ECO:0007829|PDB:1WEV"
FT STRAND 190..192
FT /evidence="ECO:0007829|PDB:1WEV"
FT HELIX 196..200
FT /evidence="ECO:0007829|PDB:1WEV"
FT HELIX 209..215
FT /evidence="ECO:0007829|PDB:1WEV"
SQ SEQUENCE 461 AA; 48568 MW; 9230385FBD4A9425 CRC64;
MAATVNLELD PIFLKALGFL HSKSKDSAEK LKALLDESLA RGIDSSYRPT QKDVEPPKIS
STKSLSIKQE PKTSSSLPSG SSNGKVLTAE KIKKEAEKRP ADKMKDVTEG IDVPKKPRLE
KPETRSSPIT VQTSKDLSMA DLSSFEETSA DDFAMEMGLA CVVCRQMTVA SGNQLVECQE
CHNLYHQDCH KPQVTDKEVN DPRLVWYCAR CTRQMKRMAQ KTQKPPQKPA PTVVSVTPTV
KDPLVKKPET KLKQETTFLA FKRTEVKPST VISGNSSSNN VSSSVTSGLT GWAAFAAKTS
SAGPSTAKLN SAAQNSSGKP AASSSNQKPV GLTGLATSSK GGIGSKIGSG NSTSPSVPLK
PLPPLTLGKT GLSRSVSCDN VSKVGLPSPS SLVPGGSSQL SGNGNSATTG PSGSTTSKAT
SETSSSTSAS LKGPTSQESQ LNAMKRLQMV KKKAAQKKLK K
